Cutting edge: tubulin α functions as an adaptor in NFAT-importin β interaction.

Upon T cell stimulation, NFAT is dephosphorylated by calcineurin, leading to nuclear translocation via NFAT-importin β interaction. Whereas the process of NFAT dephosphorylation has been well researched, the molecular mechanism of NFAT-importin β interaction remains unknown. In contrast to NF-κB and STAT, no importin α family members have been reported ...
as adaptor proteins for NFAT. Our study shows that tubulin α, but not tubulin β, binds to the N-terminal region of NFAT containing the regulatory and Rel homology domains. Importin β interacts with the NFAT-tubulin α complex rather than NFAT or tubulin α alone, resulting in cotranslocation of NFAT and tubulin α into the nucleus. Furthermore, the interaction is suppressed by acetate-induced tubulin α acetylation at lysine 40. In conclusion, tubulin α functions as an adaptor in NFAT-importin β interaction, and this function is regulated by acetate-induced acetylation.
Mesh Terms:
Acetylation, Active Transport, Cell Nucleus, Animals, Cell Nucleus, HEK293 Cells, Histone Deacetylase Inhibitors, Histone Deacetylases, Humans, Hydroxamic Acids, Jurkat Cells, Mice, Multiprotein Complexes, NFATC Transcription Factors, Protein Isoforms, Protein Transport, Sodium Acetate, Tubulin, beta Karyopherins
J. Immunol.
Date: Mar. 01, 2011
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